ID   NUOCD_SULSY             Reviewed;         576 AA.
AC   B2V8J2;
DT   16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-2008, sequence version 1.
DT   25-MAY-2022, entry version 84.
DE   RecName: Full=NADH-quinone oxidoreductase subunit C/D {ECO:0000255|HAMAP-Rule:MF_01397};
DE            EC=7.1.1.- {ECO:0000255|HAMAP-Rule:MF_01397};
DE   AltName: Full=NADH dehydrogenase I subunit C/D {ECO:0000255|HAMAP-Rule:MF_01397};
DE   AltName: Full=NDH-1 subunit C/D {ECO:0000255|HAMAP-Rule:MF_01397};
GN   Name=nuoC {ECO:0000255|HAMAP-Rule:MF_01397}; Synonyms=nuoCD, nuoD;
GN   OrderedLocusNames=SYO3AOP1_0628;
OS   Sulfurihydrogenibium sp. (strain YO3AOP1).
OC   Bacteria; Aquificae; Aquificales; Hydrogenothermaceae;
OC   Sulfurihydrogenibium; unclassified Sulfurihydrogenibium.
OX   NCBI_TaxID=436114;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YO3AOP1;
RX   PubMed=19136599; DOI=10.1128/jb.01645-08;
RA   Reysenbach A.-L., Hamamura N., Podar M., Griffiths E., Ferreira S.,
RA   Hochstein R., Heidelberg J., Johnson J., Mead D., Pohorille A.,
RA   Sarmiento M., Schweighofer K., Seshadri R., Voytek M.A.;
RT   "Complete and draft genome sequences of six members of the Aquificales.";
RL   J. Bacteriol. 191:1992-1993(2009).
CC   -!- FUNCTION: NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur
CC       (Fe-S) centers, to quinones in the respiratory chain. The immediate
CC       electron acceptor for the enzyme in this species is believed to be
CC       ubiquinone. Couples the redox reaction to proton translocation (for
CC       every two electrons transferred, four hydrogen ions are translocated
CC       across the cytoplasmic membrane), and thus conserves the redox energy
CC       in a proton gradient. {ECO:0000255|HAMAP-Rule:MF_01397}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a quinone + 5 H(+)(in) + NADH = a quinol + 4 H(+)(out) +
CC         NAD(+); Xref=Rhea:RHEA:57888, ChEBI:CHEBI:15378, ChEBI:CHEBI:24646,
CC         ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:132124;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01397};
CC   -!- SUBUNIT: NDH-1 is composed of 13 different subunits. Subunits NuoB, CD,
CC       E, F, and G constitute the peripheral sector of the complex.
CC       {ECO:0000255|HAMAP-Rule:MF_01397}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC       Rule:MF_01397}; Peripheral membrane protein {ECO:0000255|HAMAP-
CC       Rule:MF_01397}; Cytoplasmic side {ECO:0000250}.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the complex I 30 kDa
CC       subunit family. {ECO:0000255|HAMAP-Rule:MF_01397}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the complex I 49 kDa
CC       subunit family. {ECO:0000255|HAMAP-Rule:MF_01397}.
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DR   EMBL; CP001080; ACD66265.1; -; Genomic_DNA.
DR   RefSeq; WP_012459344.1; NC_010730.1.
DR   AlphaFoldDB; B2V8J2; -.
DR   SMR; B2V8J2; -.
DR   STRING; 436114.SYO3AOP1_0628; -.
DR   EnsemblBacteria; ACD66265; ACD66265; SYO3AOP1_0628.
DR   KEGG; sul:SYO3AOP1_0628; -.
DR   eggNOG; COG0649; Bacteria.
DR   eggNOG; COG0852; Bacteria.
DR   HOGENOM; CLU_015134_3_2_0; -.
DR   OMA; GGRMHYM; -.
DR   OrthoDB; 473681at2; -.
DR   GO; GO:0030964; C:NADH dehydrogenase complex; IEA:InterPro.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR   GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; IEA:InterPro.
DR   GO; GO:0048038; F:quinone binding; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.645.10; -; 1.
DR   Gene3D; 3.30.460.80; -; 1.
DR   HAMAP; MF_01397; NDH1_NuoCD_2; 1.
DR   HAMAP; MF_01358; NDH1_NuoD; 1.
DR   InterPro; IPR001135; NADH_Q_OxRdtase_suD.
DR   InterPro; IPR037232; NADH_quin_OxRdtase_su_C/D-like.
DR   InterPro; IPR001268; NADH_UbQ_OxRdtase_30kDa_su.
DR   InterPro; IPR026662; NDH-1_subunit_CD.
DR   InterPro; IPR022885; NDH1_su_D/H.
DR   InterPro; IPR029014; NiFe-Hase_large.
DR   PANTHER; PTHR11993; PTHR11993; 1.
DR   Pfam; PF00329; Complex1_30kDa; 1.
DR   Pfam; PF00346; Complex1_49kDa; 1.
DR   SUPFAM; SSF143243; SSF143243; 1.
DR   SUPFAM; SSF56762; SSF56762; 1.
PE   3: Inferred from homology;
KW   Cell inner membrane; Cell membrane; Membrane; Multifunctional enzyme; NAD;
KW   Quinone; Translocase; Transport; Ubiquinone.
FT   CHAIN           1..576
FT                   /note="NADH-quinone oxidoreductase subunit C/D"
FT                   /id="PRO_0000358702"
FT   REGION          1..176
FT                   /note="NADH dehydrogenase I subunit C"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01397"
FT   REGION          200..576
FT                   /note="NADH dehydrogenase I subunit D"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01397"
SQ   SEQUENCE   576 AA;  66728 MW;  3E7ABC971EC132F8 CRC64;
     MAWISLEKAK KLEERFGYPK VSEGKGVLSV EVPKDKFIEF LTFLKEDPEY QFKMFIDLTI
     IDHGEKENPR FQGVVILFSP KNQERIIVKT WAENETLPTL TNLWKGAKWA EREAWDMFGI
     KFEGHENLVR MLLWETYPYH PLRKDFPLEG IKDTELPSLN ETLRGENLEG LFNYDRMHTA
     LPTMEDLEIT QKKRMPVKTS QIVLNWGPLH PGTHGTIWFL FDLDGEYVKQ CDIIIGQLHR
     GVEKLGENVN WQQFIPYTDR MDYIAAINEN HAYVLAAEKM LGIEVPEKAK WIRTMMAELS
     RINSHLLWLG TYALDLGALT MFLYTFRERE KIMDIIEGIT GARFTINYFR IGGVFADLPY
     GALDAIEHLI KDLPQRINDY ETLLTRNRVW LSRNKDVCVI TEEDVYQYGL TGAVARGSGV
     PYDVRKIDKY DAYGEVEFDI PVGEKGDSYD RYLVRMEEMR QSIRIIEQCI AKLRKMSKDD
     PYFFQTPDEK KLKVTIDGRG MKLPAGETYA SSDNPRGELG FYIYNKKDGL KAHRMRIRSG
     AFYNLQVFTK AIIGRPIADA ITLLSTIDPV VGETDR